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Nat Methods. 2016 Jul;13(7):557-62. doi: 10.1038/nmeth.3891. Epub 2016 May 30.

Quantitative assessment of fluorescent proteins.

Author information

1
National High Field Magnet Lab, Florida State University, Tallahassee, Florida, USA.
2
Department of Molecular Physiology and Biophysics, Vanderbilt University, Nashville, Tennessee, USA.
3
Department of Cell Biology and Physiology, Washington University, St. Louis, Missouri, USA.
4
Erasmus Optical Imaging Centre, Josephine Nefkens Institute, Erasmus MC, Rotterdam, the Netherlands.

Abstract

The advent of fluorescent proteins (FPs) for genetic labeling of molecules and cells has revolutionized fluorescence microscopy. Genetic manipulations have created a vast array of bright and stable FPs spanning blue to red spectral regions. Common to autofluorescent FPs is their tight β-barrel structure, which provides the rigidity and chemical environment needed for effectual fluorescence. Despite the common structure, each FP has unique properties. Thus, there is no single 'best' FP for every circumstance, and each FP has advantages and disadvantages. To guide decisions about which FP is right for a given application, we have quantitatively characterized the brightness, photostability, pH stability and monomeric properties of more than 40 FPs to enable straightforward and direct comparison between them. We focus on popular and/or top-performing FPs in each spectral region.

PMID:
27240257
PMCID:
PMC4927352
DOI:
10.1038/nmeth.3891
[Indexed for MEDLINE]
Free PMC Article

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